pubmed-article:10051443 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10051443 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
pubmed-article:10051443 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:10051443 | lifeskim:mentions | umls-concept:C0206131 | lld:lifeskim |
pubmed-article:10051443 | lifeskim:mentions | umls-concept:C1622537 | lld:lifeskim |
pubmed-article:10051443 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:10051443 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:10051443 | pubmed:dateCreated | 1999-5-4 | lld:pubmed |
pubmed-article:10051443 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:abstractText | SNARE proteins are required for vesicle docking and fusion in eukaryotic cells in processes as diverse as homotypic membrane fusion and synaptic vesicle exocytosis [SNARE stands for SNAP receptor, where SNAP is soluble NSF attachment protein]. The SNARE proteins syntaxin 4 and vesicle-associated membrane protein (VAMP) 2/3 also participate in the insulin-stimulated translocation of GLUT4 from intracellular vesicles to the plasma membrane in adipose cells. We now report the molecular cloning and characterization of rat SNAP-23, a ubiquitously expressed homologue of the essential neuronal SNARE protein SNAP-25 (synaptosomal-associated protein of 25 kDa). Rat SNAP-23 is 86% and 98% identical respectively to human and mouse SNAP-23. Southern blot analysis reveals that the rat, mouse and human SNAP-23 genes encode species-specific isoforms of the same protein. Co-immunoprecipitation of syntaxin 4 and SNAP-23 shows association of these two proteins in rat adipose cell plasma membranes, and insulin stimulation does not alter the SNAP-23/syntaxin 4 complex. In addition, we demonstrate for the first time the participation of SNAP-23, along with syntaxin 4 and VAMP2/3, in the formation of 20S SNARE complexes prepared using rat adipose cell membranes and recombinant alpha-SNAP and NSF proteins. The stoichiometry of the SNARE complexes formed is essentially identical using membranes from either unstimulated or insulin-stimulated adipose cells. These data demonstrate that rat SNAP-23 associates with syntaxin 4 before insulin stimulation and is present in the SNARE complexes known to mediate the translocation of GLUT4 from intracellular vesicles to the plasma membrane of rat adipose cells. | lld:pubmed |
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pubmed-article:10051443 | pubmed:language | eng | lld:pubmed |
pubmed-article:10051443 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10051443 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10051443 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10051443 | pubmed:month | Mar | lld:pubmed |
pubmed-article:10051443 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:10051443 | pubmed:author | pubmed-author:RocheP APA | lld:pubmed |
pubmed-article:10051443 | pubmed:author | pubmed-author:CushmanS WSW | lld:pubmed |
pubmed-article:10051443 | pubmed:author | pubmed-author:St-DenisJ FJF | lld:pubmed |
pubmed-article:10051443 | pubmed:author | pubmed-author:CabaniolsJ... | lld:pubmed |
pubmed-article:10051443 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10051443 | pubmed:day | 15 | lld:pubmed |
pubmed-article:10051443 | pubmed:volume | 338 ( Pt 3) | lld:pubmed |
pubmed-article:10051443 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10051443 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10051443 | pubmed:pagination | 709-15 | lld:pubmed |
pubmed-article:10051443 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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